The biochemical effect of Ser167 phosphorylation on Chlamydomonas reinhardtii centrin.

Meyn SM, Seda C, Campbell M, Weiss KL, Hu H, Pastrana-Rios B, Chazin WJ
Biochem Biophys Res Commun. 2006 342 (1): 342-8

PMID: 16480960 · DOI:10.1016/j.bbrc.2006.01.155

Centrin is an EF-hand calcium-binding protein found in microtubule organizing centers of organisms ranging from algae and yeast to man. Phosphorylation in the centrin C-terminal domain occurs in mitosis and is associated with alterations in contractile fibers. To obtain insight into the structural basis for the functional effect of phosphorylation, Chlamydomonas reinhardtii centrin C-terminal domain phosphorylated at Ser167 (pCRC-C) has been produced and characterized. The structure of pCRC-C was compared to the unmodified protein by NMR spectroscopy. The effect of phosphorylation on target binding was examined for the complex of pCRC-C and a 19 residue centrin-binding fragment of Kar1. Remarkably, the efficient and selective phosphorylation by PKA was suppressed in the complex. Moreover, comparisons of NMR chemical shift differences induced by phosphorylation reveal a greater effect from phosphorylation in the context of the Kar1 complex than for the free protein. These results directly demonstrate that phosphorylation modulates the structure and biochemical activities of centrin.

MeSH Terms (11)

Animals Calcium-Binding Proteins Chlamydomonas reinhardtii Cyclic AMP-Dependent Protein Kinases Models, Molecular Nuclear Magnetic Resonance, Biomolecular Phosphorylation Phosphoserine Protein Binding Protein Structure, Tertiary Static Electricity

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